1GD4

SOLUTION STRUCTURE OF P25S CYSTATIN A

1GD4 の概要

• エントリーDOI: 10.2210/pdb1gd4/pdb
• 関連するPDBエントリー: 1CYU 1CYV 1GD3
• 分子名称: CYSTATIN A (1 entity in total)
• 機能のキーワード: cystatin a, thiol protease inhibitor, protein binding
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm: P01040
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 10992.39

構造登録者

Shimba, N.,Kariya, E.,Tate, S.,Kaji, H.,Kainosho, M. (登録日: 2000-09-08, 公開日: 2001-09-08, 最終更新日: 2023-12-27)

主引用文献

Shimba, N.,Kariya, E.,Tate, S.,Kaji, H.,Kainosho, M.
Structural comparison between wild-type and P25S human cystatin A by NMR spectroscopy. Does this mutation affect the a-helix conformation ?
J.STRUCT.FUNCT.GENOM., 1:26-42, 2000

PubMed Abstract: The effect of substituting Pro25, located in the alpha-helical region of the cystatin A structure, with Ser has been studied. The structures of wild type and P25S cystatin A were determined by multidimensional NMR spectroscopy under comparable conditions. These two structures were virtually identical, and the alpha-helix between Glu15-Lys30 exists with uninterrupted continuity, with a slight bend at residue 25. In order to characterize the possible substitution effects of Pro25 with Ser on the alpha-helix, the chemical shifts of the amide nitrogens and protons, the generalized order parameters obtained by the analyses of the 15N-1H relaxation data, the amide proton exchange rates, and the NOE networks among the alpha-helical and surrounding residues were carefully compared. None of these parameters indicated any significant static or dynamic structural differences between the alpha-helical regions of the wild-type and P25S cystatin A proteins. We therefore conclude that our previous structure of the wild-type cystatin A, in which the alpha-helix exhibited a sharp kink at Pro25, must be revised. The asymmetric distribution of hydrophobic interactions between the side-chain residues of the alpha-helix and the rolled beta-sheet surface, as revealed by NOEs, may be responsible for the slight bend of the alpha-helix in both variants and for the destabilized hydrogen bonding of the alpha-helical residues that follow Pro25/Ser25, as evidenced by increased amide exchange rates.

PubMed: 12836678
DOI: 10.1023/A:1011380315619

実験手法

SOLUTION NMR